The Dictyostelium essential light chain is required for myosin function
In: Cell, Jg. 69 (1992-06-12), Heft 6
Online
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Zugriff:
A Dictyostelium mutant (7-11) that expresses less than 0.5% of wild-type levels of the myosin essential light chain (EMLC) has been created by overexpression of antisense RNA. Cells from 7-11 contain wild-type levels of the myosin heavy chain (MHC) and regulatory light chain (RMLC). Myosin isolated from 7-11 cells consists of the MHC with the RMLC associated in reduced stoichiometry, and binds to purified actin in an ATP-sensitive fashion. Purified 7-11 myosin displays calcium-activated ATPase activity with a Vmax about 15%-25% of that of wild type, and a Km for ATP of 27 +/- 5 microM versus 83 +/- 30 microM for wild type. At actin concentrations as high as 17 microM, 7-11 myosin displays greatly reduced actin-activated ATPase activity. Phenotypically, 7-11 cells resemble MHC mutants, growing poorly in suspension and becoming large and multinucleate. When starved for multicellular development, 7-11 cells take several hours longer than wild-type cells to aggregate. Although multicellular aggregates eventually form, they fail to develop further. The cells are also unable to cap receptors in response to Con A treatment. Since cells expressing the EMLC are phenotypically similar to MHC null mutants, the EMLC appears necessary for myosin function, at least in part because it is required for normal actin-activated ATPase activity.
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The Dictyostelium essential light chain is required for myosin function
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Autor/in / Beteiligte Person: | Tung Ling L. Chen ; Triviños-Lagos, Leda ; Chisholm, Rex L. ; Pollenz, Richard S. |
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Zeitschrift: | Cell, Jg. 69 (1992-06-12), Heft 6 |
Veröffentlichung: | 1992 |
Medientyp: | unknown |
ISSN: | 0092-8674 (print) |
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